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Glycophorin C content of human erythrocyte membrane is regulated by protein
4.1
ME Reid, Y Takakuwa, J Conboy, G Tchernia and N Mohandas
Division of Cell and Molecular Biology, Lawrence Berkeley Laboratory,
University of California, Berkeley 94720.
Human erythrocyte transmembrane sialoglycoprotein, glycophorin C, plays a
functionally important role in maintaining erythrocyte shape and regulating
membrane material properties, possibly through its interaction with protein
4.1. Moreover, it has previously been shown that membranes deficient in
protein 4.1 exhibit decreased content of glycophorin C. To further define
the relationship between protein 4.1 and glycophorin C, a series of studies
were performed using both protein 4.1- and glycophorin C-deficient
erythrocytes. Quantitation by flow cytometry showed that the glycophorin C
content of cells totally deficient in protein 4.1 was 9% of normal and that
of cells partially deficient in protein 4.1 was 44% of normal.
Interestingly, while homozygous glycophorin C-deficient cells had no
detectable levels of this sialoglycoprotein, cells from obligate
heterozygotes had normal levels. Protein 4.1 content of membranes of these
glycophorin C- deficient cells was also normal. These data suggest that
glycophorin C may be synthesized in excess by erythroid cells and its
membrane content regulated by protein 4.1. To investigate if this
regulation is due to association between protein 4.1 and glycophorin C, we
examined the retention of glycophorin C in membrane skeletons (Triton
shells) prepared from normal membranes, protein 4.1-deficient membranes,
and protein 4.1-deficient membranes reconstituted with exogenous protein
4.1. Glycophorin C is retained by Triton shells prepared from normal
membranes, whereas Triton shells prepared from protein 4.1-deficient
membranes are totally devoid of this sialoglycoprotein. However,
reconstitution of protein 4.1-deficient membranes with purified protein 4.1
resulted in retention of glycophorin C with the Triton shells. This finding
suggests that protein 4.1 is necessary for association of glycophorin C
with the membrane skeleton. Furthermore, these data suggest that through
its interaction with glycophorin C, protein 4.1 may play a role in
regulating the membrane content of this sialoglycoprotein in mature human
erythrocytes.
Volume 75,
Issue 11,
pp. 2229-2234,
06/01/1990
Copyright © 1990 by The American Society of Hematology
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